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Caspase-9 cleavage: do you need it

By Davina Twiddy and Kelvin Cain

Abstract

This is the authors' final draft of the commentary published as Biochemical Journal, 2007, 405(1), e1-2, and available from http://www.biochemj.org/bj/405/e001/bj405e001.htmCaspase-9 which is activated by association with the Apaf-1 apoptosome complex cleaves and activates the downstream effector caspases-3 and -7, thereby executing the caspase-cascade and cell death programme. Although, caspase-9 does not need to be cleaved to be active, apoptotic cell death is always accompanied by autocatalytic cleavage and by further downstream effector caspase-dependent cleavage of caspase-9. In this issue of the Biochemical Journal, Denault and co-workers evaluate the role of caspase-3-dependent cleavage of caspase-9 and conclude that this mechanism mainly serves to enhance apoptosis by alleviating XIAP inhibition of the apical caspase

Publisher: Portland Press
Year: 2007
OAI identifier: oai:lra.le.ac.uk:2381/3370

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Citations

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